[Letter: Structural characteristics of regular polypeptides, including lysine, ornithine and proline residues].
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Circular Dichroism↗
Biomedical subjects
L I Mar'iash
Publications and source records attributed to L I Mar'iash.
[Mechanism of action of cAMP-dependent protein kinase. IV. Interaction of the enzyme catalytic subunit with structural analogs of histone H1].
A study was made of the specificity of the catalytic subunit of cAMP-dependent pig brain protein kinase with respect to structural analogs of the protein substrate, histone H1, namely: a) high-molecular-weight histone fragments obtained as the result of specific cleavage of histone with trypsin and N-bromsuccinimide; b) synthetic peptides-substrates; c) synthetic peptides-inhibitors. Analysis of the kinetic parameters estimated for these compounds allowed to evaluate the individual contribution of various elements of the primary and three-dimensional structure of histone in the processes of binding and phosphorylation. Factors of "near" and "remote" specificity in the protein substrate binding are suggested.
Animals↗
[Structure of DNA complexes with regular polypeptides].
The conformation of some regular polypeptides: (Lys-Ala)50, (Lys-Ala2)37, (Lys-Ala2)26, (Lys-Ala3)18, (Lys3-Pro)29, (Orn3-Gly)28 was studied by means of CD. The complexes of these polypeptides with DNA were obtained by the methods of jump-dilution of a two-components mixture from 2 M NaCl to 0.05 M NaCl. The extent of DNA covering by the polypeptides was compared using binding isoterms of ethidium on DNA and DNA-polypeptide complex. The length, L, which polypeptides cover on DNA was estimated by means of energy transfer between the dyes absorbed on the complexes. The CD spectra of the complexes revealed a high sensitivity to changes of the environmental conditions. Small variations in the temperature and ionic strength produces marked changes in the CD spectra of the complexes. It was suggested that observed CD changes are due to both the structural relaxation of the complexes and the existence of liquid-crystal domains in solution.
Chemical Phenomena↗